Abstract
Abstract Exploration and evaluation of lipases from different sources will always be required by the swiftly developing industries for modification of oils and fats. Lipase SMG1 from Malassezia globosa was expressed in recombinant Pichia pastoris , and its catalytic activity in the hydrolysis and synthesis of partial glycerides was evaluated. Lipase SMG1 could not hydrolyze soybean oil; however, enhanced the hydrolysis of soybean oil by combining with Palatase 20000L, suggesting it showed strict specificity on mono- and diacylglycerol. Hydrolysates of soybean oil were esterified with glycerol to produce diacylglycerol, and the optimized results for the esterification reaction were with an fatty acids/glycerol molar ratio of 1:4, lipase SMG1 at a concentration of 120 U/g (U/w, with respect to total reactants), initial water content 1% (w/w, with respect to total reactants) and 30 °C, which yielded 62.03% of diacylglycerol in reaction mixture (80.5% in acylglyceride) after 12 h of reaction. The results showed that lipase SMG1 is a prospective enzyme which could be used in the oils and fats industry.
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